ID A0A0V1H7Q1_9BILA Unreviewed; 788 AA.
AC A0A0V1H7Q1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=hydroxyacylglutathione hydrolase {ECO:0000256|ARBA:ARBA00011917};
DE EC=3.1.2.6 {ECO:0000256|ARBA:ARBA00011917};
DE AltName: Full=Glyoxalase II {ECO:0000256|ARBA:ARBA00031044};
GN Name=mkrn1 {ECO:0000313|EMBL:KRZ06386.1};
GN ORFNames=T11_13587 {ECO:0000313|EMBL:KRZ06386.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ06386.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ06386.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ06386.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid.
CC {ECO:0000256|ARBA:ARBA00004015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001623};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004963}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000256|ARBA:ARBA00006759}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ06386.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDP01000119; KRZ06386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1H7Q1; -.
DR STRING; 268475.A0A0V1H7Q1; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.30.1370.210; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR NCBIfam; TIGR03413; GSH_gloB; 1.
DR PANTHER; PTHR11935; BETA LACTAMASE DOMAIN; 1.
DR PANTHER; PTHR11935:SF94; TENZING NORGAY, ISOFORM C; 1.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR Pfam; PF14608; zf-CCCH_2; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..788
FT /note="hydroxyacylglutathione hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006878913"
FT DOMAIN 266..293
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 294..321
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 395..421
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 467..521
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 550..579
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 266..293
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 294..321
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 395..421
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 550..579
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 788 AA; 88731 MW; B65F40AB14860CB4 CRC64;
MNGIILIVIT YILLIEFKAI ENSVKMLTVI PVPALSDNYM YVLTDEERTA AAVVDPVEPR
KILNVLKQNN LTLTHVLVTH HHSDHAGGNE ELSNILHSEG LSRVKFIGGD DRIPCLNEKV
VHGQELKIGE INVLCMHTPC HTRGHICYYV TDKKDDKVVF TGDTLFIGGC GKFFEGTGRD
MYEALINRLG NLPNDTKVYC GHEYTLSNLK FALSVEPENP DLKNYMETVQ KQLDEGKFTV
PSLIGNEKKF NPFMRVMVMS ERENTPTKRV LCRYYMNGFC RHGQDCTFSH NRTDAPSMVC
RYFVRGNCTY GSRCRYDHVR PSWMLRNLEN IGFPVVNETA AKPNSDVEAA TVQLSSLRVD
APEFVPSSGV SSSASSRTYA EVVGKDETTD KDNVKKQVLC GYNVIGTCPF GEKCTYVHGD
VCDLCQRAIL IPGDEAYNST HRQECMAEHE KEMEVAFTIA RSSDKQCGIC METVMEKADE
SNRSFGILPN CKHCFCLQCI RQWRGTNEFD LKNTRACPEC RVMSDFVVPS SFWVETAEER
ACLIDSYKSS LKQRRCKYYV HGQRECQFGN KCFYRHEDPE GRLVEGDSPR TIRRRMRRMN
RNRRRQSNHF RRDFIYLGRF MEAAIVNDDI TEALNDILDE SGGEDYFPSD SDDDYYTWLH
PEWHTCRIQQ HALLFESELI ASTTSSTTTT LDEEGVATAA AAAAVAVSRF TNGDPVVVMG
DDSRIGCLME AAPRPTSDDG MFGDGGTGRR FFGEISCDAA DLGDGQPSFD GAIMCATDSV
ATDETKQN
//
